ID   F4QHR0_9CAUL            Unreviewed;       329 AA.
AC   F4QHR0;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=D-ala D-ala ligase protein {ECO:0000313|EMBL:EGF92797.1};
GN   ORFNames=ABI_12350 {ECO:0000313|EMBL:EGF92797.1};
OS   Asticcacaulis biprosthecium C19.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=715226 {ECO:0000313|EMBL:EGF92797.1, ECO:0000313|Proteomes:UP000006512};
RN   [1] {ECO:0000313|Proteomes:UP000006512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C19 {ECO:0000313|Proteomes:UP000006512};
RA   Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Draft genome sequence of Brevundimonas diminuta.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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DR   EMBL; GL883077; EGF92797.1; -; Genomic_DNA.
DR   RefSeq; WP_006271979.1; NZ_GL883077.1.
DR   AlphaFoldDB; F4QHR0; -.
DR   STRING; 715226.ABI_12350; -.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_039268_1_1_5; -.
DR   OrthoDB; 9813261at2; -.
DR   Proteomes; UP000006512; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR011095; Dala_Dala_lig_C.
DR   InterPro; IPR011127; Dala_Dala_lig_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR23132:SF23; D-ALANINE--D-ALANINE LIGASE B; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF01820; Dala_Dala_lig_N; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Ligase {ECO:0000313|EMBL:EGF92797.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN          128..321
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   329 AA;  35037 MW;  18D82973FC6D5C30 CRC64;
     MKPTILFGGT SRERLVSVAS AQALAHALPD ADLWFWDHDG TVNVTSPAAL HAHDRPFELP
     FRADGILIGD MAGSLDLAVH ENRVLVLGLH GGSAENGEFQ VLAEARGVPF TGSGSAASHL
     AFDKTAAKRF AGLAGVHSPS SVSLDELDEA FSHYGKLIAK PAQDGSSFGL IYVNSSQDLA
     AVRREAKTTA YVIEPFVTGP EATCGVLEQA DGSLIALPPV EIVPAEGTFD YKSKYLAAAT
     QEICPARFAS EIMAQLRDLS IKAHKAMSCR GYSRSDFIIS DHGPVYLETN TLPGLTKASL
     YPKSLKAQGI EFVDFLNGQI ELAVKRAGR
//